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Brown, MA, Sims, RJ 3rd, Gottlieb, PD and Tucker, PW (2006) Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol. Cancer 5:26
Disrupting the balance of histone lysine methylation alters the expression of genes involved in tumorigenesis including proto-oncogenes and cell cycle regulators. Methylation of lysine residues is commonly catalyzed by a family of proteins that contain the SET domain. Here, we report the identification and characterization of the SET domain-containing protein, Smyd2.
Amino Acid Sequence; Animals; Cell Line; Chromatin/chemistry; Gene Expression Regulation; Histone-Lysine N-Methyltransferase/chemistry; Histone-Lysine N-Methyltransferase/physiology; Histones/chemistry; Humans; Lysine/chemistry; Methyltransferases/biosynthesis; Methyltransferases/chemistry; Mice; Molecular Sequence Data; NIH 3T3 Cells; Protein Structure, Tertiary; Repressor Proteins/chemistry; Sequence Homology, Amino Acid